ID A0A2W1MZH7_9FLAO Unreviewed; 845 AA.
AC A0A2W1MZH7;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit {ECO:0000313|EMBL:PZE17629.1};
GN ORFNames=DNU06_07310 {ECO:0000313|EMBL:PZE17629.1};
OS Putridiphycobacter roseus.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Crocinitomicaceae; Putridiphycobacter.
OX NCBI_TaxID=2219161 {ECO:0000313|EMBL:PZE17629.1, ECO:0000313|Proteomes:UP000249248};
RN [1] {ECO:0000313|EMBL:PZE17629.1, ECO:0000313|Proteomes:UP000249248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM1701 {ECO:0000313|EMBL:PZE17629.1,
RC ECO:0000313|Proteomes:UP000249248};
RA Zhang X.;
RT "The draft genome sequence of Crocinitomix sp. SM1701.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|RuleBase:RU004432}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PZE17629.1}.
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DR EMBL; QKSB01000003; PZE17629.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2W1MZH7; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000249248; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00009; AAA; 1.
DR CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR Gene3D; 1.10.8.60; -; 2.
DR Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 4.10.860.10; UVR domain; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR019489; Clp_ATPase_C.
DR InterPro; IPR036628; Clp_N_dom_sf.
DR InterPro; IPR004176; Clp_R_dom.
DR InterPro; IPR001270; ClpA/B.
DR InterPro; IPR018368; ClpA/B_CS1.
DR InterPro; IPR028299; ClpA/B_CS2.
DR InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001943; UVR_dom.
DR PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR PANTHER; PTHR11638:SF18; HEAT SHOCK PROTEIN 104; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF17871; AAA_lid_9; 1.
DR Pfam; PF02861; Clp_N; 2.
DR Pfam; PF10431; ClpB_D2-small; 1.
DR PRINTS; PR00300; CLPPROTEASEA.
DR SMART; SM00382; AAA; 2.
DR SMART; SM01086; ClpB_D2-small; 1.
DR SUPFAM; SSF81923; Double Clp-N motif; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51903; CLP_R; 1.
DR PROSITE; PS00870; CLPAB_1; 1.
DR PROSITE; PS00871; CLPAB_2; 1.
DR PROSITE; PS50151; UVR; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004432};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU004432};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000313|EMBL:PZE17629.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:PZE17629.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000249248};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 1..146
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT DOMAIN 442..477
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 146..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 431..484
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 153..187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 845 AA; 95039 MW; C3E334EC83478F8F CRC64;
MDANFSSKAK NVIAYSREEA LRLGNDYLGV EHLLLGLLRE KESLAVKILQ EFHLDLEVLR
KDIEKNVKES TNKPIDAKNI PLVRQAEKVL KITYLESRLF KSANVGTEHI LLAILREKDN
IATRILNKYG VIYENVKEEL EEMIDEENTP KSEFPGGISN DDSSSESTNF GSGSSASKGN
NKSKTPVLDN FGRDLTAMAE QDKLDPIVGR HQEIERVSQI LSRRKKNNPI LIGEPGVGKS
AIAEGLALRI VQRKVSRVLF GKRVISLDLA SLVAGTKYRG QFEERMKAVM NELEKSRDVI
LFIDEIHTII GAGGASGSMD ASNMFKPALA RGEIQVIGAT TLDEFRQYVE KDGALERRFQ
KVLIEPTTIE ESIEILTNIK ERYEDHHNVS YTPEAISACV RLTERYMSDR NLPDKAIDAM
DEVGSRVHIK NINVPKEIKS LEEQIEKIKE EKNNVIKSQK YEKAAELRDT EKKLQDDLET
AQIKWEEDAK LNRIVVNEEH VAEVVSMMTG IPLQKVSESE SGKIIHLADD IAKGVIGQDE
AIKKVVKAIQ RNRAGLKDPN KPIGSFFFLG PTGVGKTRLA KVLAKNLFDS EDALIRIDMS
EYMEKFSVSR LVGAPPGYVG YEEGGQLTEK VRRKPYSIIL LDEIEKAHPD VFNMLLQVLD
DGHMTDGLGR KIDFKNTIII MTSNIGVRQL QDFGTGVGFG TAAKNEQKDE AAIVIIQKAL
KKAFAPEFLN RIDDMIIFNS LKPEHIYKII DIELVKLFGR ITELGYKTEI TDEAKKFIAD
KGYDNKYGAR PLNRAIQKYI EDPLAEEIIN SNIKENDIIK IDFDKKEEKI DISIVKGKSK
KTESK
//